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Inosine-5'-monophosphate dehydrogenase 3 (IMP dehydrogenase 3) (IMPD 3) (IMPDH 3) (EC 1.1.1.205)

 IMDH3_YEAST             Reviewed;         523 AA.
P50095; D6VZ67;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 169.
RecName: Full=Inosine-5'-monophosphate dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMP dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPD 3 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPDH 3 {ECO:0000255|HAMAP-Rule:MF_03156};
EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03156};
Name=IMD3 {ECO:0000255|HAMAP-Rule:MF_03156};
OrderedLocusNames=YLR432W; ORFNames=L9753.4;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
FUNCTION.
PubMed=12746440; DOI=10.1074/jbc.M303736200;
Hyle J.W., Shaw R.J., Reines D.;
"Functional distinctions between IMP dehydrogenase genes in providing
mycophenolate resistance and guanine prototrophy to yeast.";
J. Biol. Chem. 278:28470-28478(2003).
[6]
FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15292516; DOI=10.1073/pnas.0403341101;
McPhillips C.C., Hyle J.W., Reines D.;
"Detection of the mycophenolate-inhibited form of IMP dehydrogenase in
vivo.";
Proc. Natl. Acad. Sci. U.S.A. 101:12171-12176(2004).
[7]
FUNCTION, AND MUTAGENESIS OF ALA-253.
PubMed=16278936; DOI=10.1002/yea.1300;
Jenks M.H., Reines D.;
"Dissection of the molecular basis of mycophenolate resistance in
Saccharomyces cerevisiae.";
Yeast 22:1181-1190(2005).
-!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP)
to xanthosine 5'-phosphate (XMP), the first committed and rate-
limiting step in the de novo synthesis of guanine nucleotides, and
therefore plays an important role in the regulation of cell
growth. {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:12746440, ECO:0000269|PubMed:15292516,
ECO:0000269|PubMed:16278936}.
-!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
xanthosine 5'-phosphate + NADH. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000255|HAMAP-Rule:MF_03156};
-!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive
inhibitor that prevents formation of the closed enzyme
conformation by binding to the same site as the amobile flap. In
contrast, mizoribine monophosphate (MZP) is a competitive
inhibitor that induces the closed conformation. MPA is a potent
inhibitor of mammalian IMPDHs but a poor inhibitor of the
bacterial enzymes. MZP is a more potent inhibitor of bacterial
IMPDH. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=100 uM for Inosine 5'-phosphate
{ECO:0000269|PubMed:15292516};
KM=314 uM for NAD(+) {ECO:0000269|PubMed:15292516};
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- SUBUNIT: Homotetramer. Seems to be able to form heterotetramers
composed from more than 1 of the 3 IMPDH gene products (IMD2-4).
{ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:15292516}.
-!- INTERACTION:
P50094:IMD4; NbExp=6; IntAct=EBI-9190, EBI-9195;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 26300 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
Rule:MF_03156}.
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EMBL; U21094; AAB67516.1; -; Genomic_DNA.
EMBL; BK006945; DAA09733.1; -; Genomic_DNA.
PIR; S59402; S59402.
RefSeq; NP_013536.3; NM_001182320.3.
ProteinModelPortal; P50095; -.
SMR; P50095; -.
BioGrid; 31691; 167.
DIP; DIP-1947N; -.
IntAct; P50095; 199.
MINT; MINT-385605; -.
STRING; 4932.YLR432W; -.
MaxQB; P50095; -.
PRIDE; P50095; -.
EnsemblFungi; YLR432W; YLR432W; YLR432W.
GeneID; 851152; -.
KEGG; sce:YLR432W; -.
EuPathDB; FungiDB:YLR432W; -.
SGD; S000004424; IMD3.
GeneTree; ENSGT00900000141210; -.
HOGENOM; HOG000165752; -.
KO; K00088; -.
OMA; NLGSQNR; -.
OrthoDB; EOG092C1U8P; -.
BioCyc; YEAST:YLR432W-MONOMER; -.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis.
Reactome; R-SCE-74217; Purine salvage.
SABIO-RK; P50095; -.
UniPathway; UPA00601; UER00295.
PRO; PR:P50095; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0003938; F:IMP dehydrogenase activity; TAS:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006183; P:GTP biosynthetic process; TAS:SGD.
CDD; cd00381; IMPDH; 1.
Gene3D; 3.20.20.70; -; 2.
HAMAP; MF_01964; IMPDH; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005990; IMP_DH.
InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
InterPro; IPR001093; IMP_DH_GMPRt.
Pfam; PF00571; CBS; 2.
Pfam; PF00478; IMPDH; 1.
PIRSF; PIRSF000130; IMPDH; 1.
SMART; SM00116; CBS; 2.
TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
PROSITE; PS51371; CBS; 2.
PROSITE; PS00487; IMP_DH_GMP_RED; 1.
1: Evidence at protein level;
CBS domain; Complete proteome; Cytoplasm; GMP biosynthesis;
Metal-binding; NAD; Oxidoreductase; Potassium; Purine biosynthesis;
Reference proteome; Repeat.
CHAIN 1 523 Inosine-5'-monophosphate dehydrogenase 3.
/FTId=PRO_0000093683.
DOMAIN 121 183 CBS 1. {ECO:0000255|HAMAP-Rule:MF_03156}.
DOMAIN 184 240 CBS 2. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 278 280 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 328 330 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
REGION 368 370 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03156}.
REGION 391 392 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03156}.
REGION 415 419 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03156}.
ACT_SITE 335 335 Thioimidate intermediate.
{ECO:0000255|HAMAP-Rule:MF_03156}.
ACT_SITE 437 437 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03156}.
METAL 330 330 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 332 332 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 335 335 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 508 508 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 509 509 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 510 510 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
BINDING 333 333 IMP. {ECO:0000255|HAMAP-Rule:MF_03156}.
BINDING 449 449 IMP. {ECO:0000255|HAMAP-Rule:MF_03156}.
MUTAGEN 253 253 A->S: Increases drug-resistance to MPA.
{ECO:0000269|PubMed:16278936}.
SEQUENCE 523 AA; 56585 MW; A0C84C22527AAEA6 CRC64;
MAAVRDYKTA LEFAKSLPRL DGLSVQELMD SKTRGGLTYN DFLVLPGLVD FPSSEVSLQT
KLTRNITLNT PFVSSPMDTV TESEMAIFMA LLGGIGFIHH NCTPEDQADM VRRVKNYENG
FINNPIVISP TTTVGEAKSM KERFGFSGFP VTEDGKRNGK LMGIVTSRDI QFVEDNSLLV
QDVMTKNPVT GAQGITLSEG NEILKKIKKG KLLIVDDNGN LVSMLSRTDL MKNQNYPLAS
KSATTKQLLC GAAIGTIDAD KERLRLLVEA GLDVVILDSS QGNSIFQLNM IKWIKETFPD
LEIIAGNVAT REQAANLIAA GADGLRIGMG SGSICITQEV MACGRPQGTA VYNVCEFANQ
FGIPCMADGG VQNIGHITKA LALGSSTVMM GGMLAGTTES PGEYFYQDGK RLKAYRGMGS
IDAMQKTGTK GNASTSRYFS ESDSVLVAQG VSGAVVDKGS IKKFIPYLYN GLQHSCQDIG
YKSLTLLKEN VQSGKVRFEF RTASAQLEGG VHNLHSYEKR LHN


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